Family: Cytochrome c oxidase Subunit F

membrane-anchored rubredoxin-like domain

Lineage:

1. Root: scop
2. Class: Small proteins [56992]
   Usually dominated by metal ligand, heme, and/or disulfide bridges
3. Fold: Rubredoxin-like [57769]
   metal(zinc or iron)-bound fold; sequence contains two CX(n)C motifs, in most cases n = 2
4. Superfamily: Rubredoxin-like [57802]
   uperfamily
5. Family: Cytochrome c oxidase Subunit F [57818]
   membrane-anchored rubredoxin-like domain

Protein Domains:

1. Cytochrome c oxidase Subunit F [57819]
   1. Cow (Bos taurus) [TaxId: 9913] [57820] (21)
      1. 1v54
         complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, unx, zn
         1. chain f [100327]
         2. chain s [100341]
      2. 2dyr
         automatically matched to d1occf_
         complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, unx, zn
         1. region f:1-98 [131905]
      3. 2dyr
         automatically matched to d1occf_
         complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, unx, zn
         1. region s:1-98 [131919]
      4. 1v55
         complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, unx, zn
         1. chain f [100355]
         2. chain s [100369]
      5. 2eij
         automatically matched to d1occf_
         complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
         1. region f:1-98 [132145]
      6. 2eij
         automatically matched to d1occf_
         complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
         1. region s:1-98 [132159]
      7. 2eil
         automatically matched to d1occf_
         complexed with cd, cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
         1. region f:1-98 [132201]
      8. 2eil
         automatically matched to d1occf_
         complexed with cd, cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
         1. region s:1-98 [132215]
      9. 2eik
         automatically matched to d1occf_
         complexed with cd, cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
         1. region f:1-98 [132173]
      10. 2eik
          automatically matched to d1occf_
          complexed with cd, cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
          1. region s:1-98 [132187]
      11. 2dys
          automatically matched to d1occf_
          complexed with cdl, chd, cu, cua, dmu, glh, hea, mg, na, pek, pgv, psc, tgl, unx, zn
          1. region f:1-98 [131933]
      12. 2dys
          automatically matched to d1occf_
          complexed with cdl, chd, cu, cua, dmu, glh, hea, mg, na, pek, pgv, psc, tgl, unx, zn
          1. region s:1-98 [131947]
      13. 2occ
          complexed with cu, hea, mg, na, per, zn
          1. chain f [45256]
          2. chain s [45257]
      14. 1ocr
          complexed with cu, hea, mg, na, zn
          1. chain f [45258]
          2. chain s [45259]
      15. 2eim
          automatically matched to d1occf_
          complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
          1. region f:1-98 [132229]
      16. 2eim
          automatically matched to d1occf_
          complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
          1. region s:1-98 [132243]
      17. 2ein
          automatically matched to d1occf_
          complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
          1. region f:1-98 [132257]
      18. 2ein
          automatically matched to d1occf_
          complexed with cdl, chd, cu, cua, dmu, hea, mg, na, pek, pgv, psc, tgl, zn
          1. region s:1-98 [132271]
      19. 1occ
          complexed with cu, hea, mg, zn
          1. chain f [45260]
          2. chain s [45261]
      20. 1ocz
          complexed with azi, cu, hea, mg, na, zn
          1. chain f [45262]
          2. chain s [45263]
      21. 1oco
          complexed with cmo, cu, hea, mg, na, zn
          1. chain f [45264]
          2. chain s [45265]

Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009 Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk